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Proclavaminate amidinohydrolase

In enzymology, a proclavaminate amidinohydrolase (EC 3.5.3.22) is an enzyme that catalyzes the chemical reaction

Proclavaminate amidinohydrolase
Identifiers
EC no.3.5.3.22
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
amidinoproclavaminate + H2O proclavaminate + urea

Thus, the two substrates of this enzyme are amidinoproclavaminate and H2O, whereas its two products are proclavaminate and urea.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is amidinoproclavaminate amidinohydrolase. Other names in common use include PAH, and proclavaminate amidino hydrolase. This enzyme participates in clavulanic acid biosynthesis.

References edit

  • Salowe SP, Krol WJ, Iwata-Reuyl D, Townsend CA (1991). "Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction". Biochemistry. 30 (8): 2281–92. doi:10.1021/bi00222a034. PMID 1998687.
  • Zhou J, Kelly WL, Bachmann BO, Gunsior M, Townsend CA (2001). "Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional alpha-KG-dependent non-heme iron enzyme: correlation with mechanisms and reactivities". J. Am. Chem. Soc. 123 (30): 7388–98. doi:10.1021/ja004025+. PMID 11472170.
  • Townsend CA (2002). "New reactions in clavulanic acid biosynthesis". Curr. Opin. Chem. Biol. 6 (5): 583–9. doi:10.1016/S1367-5931(02)00392-7. PMID 12413541.
  • Wu TK, Busby RW, Houston TA, McIlwaine DB, Egan LA, Townsend CA (1995). "Identification, cloning, sequencing, and overexpression of the gene encoding proclavaminate amidino hydrolase and characterization of protein function in clavulanic acid biosynthesis". J. Bacteriol. 177 (13): 3714–20. PMC 177087. PMID 7601835.


proclavaminate, amidinohydrolase, enzymology, proclavaminate, amidinohydrolase, enzyme, that, catalyzes, chemical, reactionidentifiersec, 22databasesintenzintenz, viewbrendabrenda, entryexpasynicezyme, viewkeggkegg, entrymetacycmetabolic, pathwaypriamprofilepd. In enzymology a proclavaminate amidinohydrolase EC 3 5 3 22 is an enzyme that catalyzes the chemical reactionProclavaminate amidinohydrolaseIdentifiersEC no 3 5 3 22DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins amidinoproclavaminate H2O displaystyle rightleftharpoons proclavaminate ureaThus the two substrates of this enzyme are amidinoproclavaminate and H2O whereas its two products are proclavaminate and urea This enzyme belongs to the family of hydrolases those acting on carbon nitrogen bonds other than peptide bonds specifically in linear amidines The systematic name of this enzyme class is amidinoproclavaminate amidinohydrolase Other names in common use include PAH and proclavaminate amidino hydrolase This enzyme participates in clavulanic acid biosynthesis References editSalowe SP Krol WJ Iwata Reuyl D Townsend CA 1991 Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction Biochemistry 30 8 2281 92 doi 10 1021 bi00222a034 PMID 1998687 Zhou J Kelly WL Bachmann BO Gunsior M Townsend CA 2001 Spectroscopic studies of substrate interactions with clavaminate synthase 2 a multifunctional alpha KG dependent non heme iron enzyme correlation with mechanisms and reactivities J Am Chem Soc 123 30 7388 98 doi 10 1021 ja004025 PMID 11472170 Townsend CA 2002 New reactions in clavulanic acid biosynthesis Curr Opin Chem Biol 6 5 583 9 doi 10 1016 S1367 5931 02 00392 7 PMID 12413541 Wu TK Busby RW Houston TA McIlwaine DB Egan LA Townsend CA 1995 Identification cloning sequencing and overexpression of the gene encoding proclavaminate amidino hydrolase and characterization of protein function in clavulanic acid biosynthesis J Bacteriol 177 13 3714 20 PMC 177087 PMID 7601835 Portal nbsp Biology This EC 3 5 enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Proclavaminate amidinohydrolase amp oldid 1172358238, wikipedia, wiki, book, books, library,

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